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FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation

Authors :
Dailu Chen
Sofia Bali
Ruhar Singh
Aleksandra Wosztyl
Vishruth Mullapudi
Jaime Vaquer-Alicea
Parvathy Jayan
Shamiram Melhem
Harro Seelaar
John C. van Swieten
Marc I. Diamond
Lukasz A. Joachimiak
Source :
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)
Publication Year :
2023
Publisher :
Nature Portfolio, 2023.

Abstract

The authors used multi-disciplinary approaches to understand the structural mechanism underlying spontaneous aggregation of tau encoding an S320F FTD-tau mutant. Understanding the mechanisms of tau aggregation will help identify novel methods to regulate its misfolding.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
14
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.b84963259f3d4cf7b3feeba89b86ffa0
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-023-37274-6